The birth of a new field
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Spence, John C. H.; Chapman, Henry N.

doi:10.1098/rstb.2013.0309

Cited by 32 publications

(28 citation statements)

References 26 publications

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“…The recent advent of femtosecond serial crystallography has demonstrated the capability of collecting complete, high-quality data sets from samples of micrometer or sub-micrometer sized crystals. [10a,19] This approach, however, often requires vast quantities of sample owing to the low efficiency (hit-rate) of the sample delivery system. Acoustic methods, such as those detailed herein, promise to significantly increase the efficiency and throughput of serial crystallography methods as well as more conventional screening and data collection approaches.…”

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confidence: 99%

Precise Manipulation and Patterning of Protein Crystals for Macromolecular Crystallography Using Surface Acoustic Waves

Guo

Zhou

et al. 2015

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Advances in modern X-ray sources and detector technology have made it possible for crystallographers to collect usable data on crystals of only a few micrometers or less in size. Despite these developments, sample handling techniques have significantly lagged behind and often prevent the full realization of current beamline capabilities. In order to address this shortcoming we have developed a surface acoustic wave-based method for manipulating and patterning crystals. This method, which does not damage the fragile protein crystals, can precisely manipulate and pattern micrometer and sub-micrometer sized crystals for data collection and screening. The technique is robust, inexpensive, and easy to implement. This method not only promises to significantly increase efficiency and throughput of both conventional and serial crystallography experiments, but also will make it possible to collect data on samples that were previously intractable.

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confidence: 99%

Precise Manipulation and Patterning of Protein Crystals for Macromolecular Crystallography Using Surface Acoustic Waves

Guo

Zhou

et al. 2015

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“…The awareness brought about by the spectacular achievements in ultrafast electron-based science have surely cross-fertilized the field of ultrafast X-ray science, which has been marked by no less spectacular achievements 178 . This is becoming more evident with the development of X-ray free electron lasers (XFELs), 179–181 which are based on high energy electron accelerators. We are even witnessing a convergence of the two branches of ultrafast structural dynamics with several groups increasingly using the MeV electron pulses from XFELs, which have the advantage of overcoming space charge due to their relativistic speeds 182,183 .…”

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confidence: 99%

From structure to structural dynamics: Ahmed Zewail's legacy

Chergui

Thomas

2017

Structural Dynamics

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In this brief tribute to Ahmed Zewail, we highlight and place in the historical context, several of the major achievements that he and his colleagues have made in Femtochemistry (of which he was the principal instigator) and his introduction of ultrafast electron scattering, diffraction, microscopy and spectroscopy. By achieving a sub-picosecond temporal resolution, coupled with a picometer spatial resolution, he revolutionised our understanding of the corpus of chemical, physical, biological and materials science systems.

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“…The first experiments illuminated a path to achieve room-temperature structures free of radiation damage, from samples too small to provide useful data at synchrotron facilities, as well as providing the means to carry out time-resolved crystallography at femtoseconds to milliseconds. In the five years since, progress has been substantial and rapid, invigorating the field of macromolecular crystallography [4,5]. This phase of development is far from over, but with both the LCLS and the Spring-8 Ångström Compact Free-electron Laser (SACLA) providing facilities for measurements, the benefits of X-ray FELs are already being translated into new biological insights.…”

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Serial Femtosecond Crystallography

Chapman

2015

Synchrotron Radiation News

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X-ray free-electron lasers produce brief flashes of X-rays that are of about a billion times higher peak brightness than achievable from storage ring sources. Such a tremendous jump in X-ray source capabilities, that came in 2009 when the Linac Coherent Light Source begun operations, was unprecedented in the history of X-ray science. Protein structure determination through the method of macromolecular crystallography has consistently benefited from the many increases in source performance from rotating anodes to all generations of synchrotron facilities. But when confronted with the prospects of such bright beams for structural biology, enthusiastic proposals were tempered by a trepidation of the effects of such beams on samples and challenges to record data [1]. A decade after these discussions (and others in USA) on the applications of X-ray FELs for biology, the first experiments took place at LCLS giving results that fulfilled many of the dreams of the early visionaries. In particular, the concept that diffraction representing the pristine object could be recorded before the Xray pulse completely vaporises the object was validated [2], confirming predictions [3] that established dose limits could be vastly exceeded using femtosecond-duration pulses. The first experiments illuminated a path to achieve room-temperature structures free of radiation damage, from samples too small to provide useful data at synchrotron facilities, as well as providing the means to carry out time-resolved crystallography at femtoseconds to milliseconds. In the five years since, progress has been substantial and rapid, invigorating the field of macromolecular crystallography [4,5]. This phase of development is far from over, but with both the LCLS and the Spring-8 Ångström Compact Free-electron Laser (SACLA) providing facilities for measurements, the benefits of X-ray FELs are already being translated into new biological insights.One of the main bottlenecks in protein structure determination is the need for large welldiffracting crystals of the protein of interest, which can take months or years of effort to achieve, if at all. Smaller crystals should be easier to obtain, given that showers of small crystals are often observed in crystallisation trials. For a fixed defect density, the likelihood to obtain a portion of well ordered crystals should increase as their volume decreases. The strength of a diffraction pattern of such an ideal crystal is proportional to the number of unit cells, and thus the volume, of the crystal. It is also proportional to the

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The birth of a new field

Abstract: One contribution of 27 to a Discussion Meeting Issue 'Biology with free-electron X-ray lasers'.

Cited by 32 publications

References 26 publications

Precise Manipulation and Patterning of Protein Crystals for Macromolecular Crystallography Using Surface Acoustic Waves

Precise Manipulation and Patterning of Protein Crystals for Macromolecular Crystallography Using Surface Acoustic Waves

From structure to structural dynamics: Ahmed Zewail's legacy

Serial Femtosecond Crystallography

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